Creatine kinase is an enzyme found in rapidly respiring tissues such as heart, muscle and brain. It is a well-studied enzyme, but to date, there is no X-ray crystal solution for the enzyme. In collaboration with Professor Robert Stroud here at UCSF, we are trying to accomplish this goal. In lieu of a three-dimensional structure, we are utilizing mutagenesis and homology studies to try to identify amino acid residues that may be important in substrate binding and catalysis. It has come to our attention that the crystal structure of a structural homolog will soon become available. The Computer Graphic Laboratory will be an indispensable asset in this regard, as it will provide us the means and resources through which we can carry on even more meaningful investigations in this research. The Computer Graphics Laboratory also provides another important asset, allowing us to access numerous databases and search for proteins that show similarity to creatine kinase. By aligning these protein sequences using programs provided by CGL, we may be able to find amino acid residues that may be conserved throughout evolution. This information allows us to assess the importance of the various amino acid residues with respect to substrate binding and catalysis. We then use site-specific mutagenesis to test our hypotheses concerning specific amino acid residues. We have already done so in one instance, and may have determined the locale of an important residue in the active site of creatine kinase.